ZN326_HUMAN
ID ZN326_HUMAN Reviewed; 582 AA.
AC Q5BKZ1; A8MYX1; B4DLN0; B4E179; Q5VW93; Q5VW94; Q5VW96; Q5VW97; Q6NSA2;
AC Q7Z638; Q7Z6C2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DBIRD complex subunit ZNF326;
DE AltName: Full=Zinc finger protein 326;
DE AltName: Full=Zinc finger protein interacting with mRNPs and DBC1;
GN Name=ZNF326; Synonyms=ZIRD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Kidney, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP IDENTIFICATION IN THE DBIRD COMPLEX, FUNCTION, AND INTERACTION WITH CCAR2.
RX PubMed=22446626; DOI=10.1038/nature10925;
RA Close P., East P., Dirac-Svejstrup A.B., Hartmann H., Heron M., Maslen S.,
RA Chariot A., Soding J., Skehel M., Svejstrup J.Q.;
RT "DBIRD complex integrates alternative mRNA splicing with RNA polymerase II
RT transcript elongation.";
RL Nature 484:386-389(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-56; SER-63; SER-81;
RP SER-82; SER-91; SER-114; SER-118; SER-121; SER-212; SER-249; THR-251 AND
RP SER-270, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-69 AND SER-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-173 AND ARG-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-140; LYS-240; LYS-247; LYS-254;
RP LYS-264; LYS-401; LYS-459 AND LYS-467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Core component of the DBIRD complex, a multiprotein complex
CC that acts at the interface between core mRNP particles and RNA
CC polymerase II (RNAPII) and integrates transcript elongation with the
CC regulation of alternative splicing: the DBIRD complex affects local
CC transcript elongation rates and alternative splicing of a large set of
CC exons embedded in (A + T)-rich DNA regions. May play a role in neuronal
CC differentiation and is able to bind DNA and activate expression in
CC vitro. {ECO:0000269|PubMed:22446626}.
CC -!- SUBUNIT: Component of the DBIRD complex. Interacts with CCAR2; the
CC interaction is direct. {ECO:0000269|PubMed:22446626}.
CC -!- INTERACTION:
CC Q5BKZ1; O60477: BRINP1; NbExp=5; IntAct=EBI-2560158, EBI-3904864;
CC Q5BKZ1; P57678: GEMIN4; NbExp=3; IntAct=EBI-2560158, EBI-356700;
CC Q5BKZ1; P13807: GYS1; NbExp=3; IntAct=EBI-2560158, EBI-740553;
CC Q5BKZ1; O75525: KHDRBS3; NbExp=3; IntAct=EBI-2560158, EBI-722504;
CC Q5BKZ1; P02549: SPTA1; NbExp=3; IntAct=EBI-2560158, EBI-375617;
CC Q5BKZ1; Q2NL98: VMAC; NbExp=3; IntAct=EBI-2560158, EBI-2803134;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5BKZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BKZ1-2; Sequence=VSP_014956;
CC Name=3;
CC IsoId=Q5BKZ1-3; Sequence=VSP_043772;
CC -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01140}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52645.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH70341.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK297073; BAG59592.1; -; mRNA.
DR EMBL; AK303707; BAG64691.1; -; mRNA.
DR EMBL; AL161797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73125.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73128.1; -; Genomic_DNA.
DR EMBL; BC052645; AAH52645.1; ALT_SEQ; mRNA.
DR EMBL; BC053888; AAH53888.1; -; mRNA.
DR EMBL; BC070341; AAH70341.1; ALT_SEQ; mRNA.
DR EMBL; BC090866; AAH90866.1; -; mRNA.
DR CCDS; CCDS727.1; -. [Q5BKZ1-1]
DR CCDS; CCDS728.1; -. [Q5BKZ1-2]
DR RefSeq; NP_001307114.1; NM_001320185.1.
DR RefSeq; NP_861446.2; NM_181781.3. [Q5BKZ1-3]
DR RefSeq; NP_892020.1; NM_182975.3. [Q5BKZ1-2]
DR RefSeq; NP_892021.1; NM_182976.3. [Q5BKZ1-1]
DR RefSeq; XP_005270836.1; XM_005270779.4. [Q5BKZ1-3]
DR RefSeq; XP_011539592.1; XM_011541290.2. [Q5BKZ1-3]
DR AlphaFoldDB; Q5BKZ1; -.
DR BioGRID; 129936; 156.
DR CORUM; Q5BKZ1; -.
DR IntAct; Q5BKZ1; 63.
DR MINT; Q5BKZ1; -.
DR STRING; 9606.ENSP00000340796; -.
DR GlyGen; Q5BKZ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5BKZ1; -.
DR PhosphoSitePlus; Q5BKZ1; -.
DR BioMuta; ZNF326; -.
DR DMDM; 73622105; -.
DR EPD; Q5BKZ1; -.
DR jPOST; Q5BKZ1; -.
DR MassIVE; Q5BKZ1; -.
DR MaxQB; Q5BKZ1; -.
DR PaxDb; Q5BKZ1; -.
DR PeptideAtlas; Q5BKZ1; -.
DR PRIDE; Q5BKZ1; -.
DR ProteomicsDB; 62713; -. [Q5BKZ1-1]
DR ProteomicsDB; 62714; -. [Q5BKZ1-2]
DR ProteomicsDB; 62715; -. [Q5BKZ1-3]
DR Antibodypedia; 19855; 143 antibodies from 23 providers.
DR DNASU; 284695; -.
DR Ensembl; ENST00000340281.9; ENSP00000340796.4; ENSG00000162664.17. [Q5BKZ1-1]
DR Ensembl; ENST00000361911.9; ENSP00000355318.5; ENSG00000162664.17. [Q5BKZ1-2]
DR GeneID; 284695; -.
DR KEGG; hsa:284695; -.
DR MANE-Select; ENST00000340281.9; ENSP00000340796.4; NM_182976.4; NP_892021.1.
DR UCSC; uc001dnp.5; human. [Q5BKZ1-1]
DR CTD; 284695; -.
DR DisGeNET; 284695; -.
DR GeneCards; ZNF326; -.
DR HGNC; HGNC:14104; ZNF326.
DR HPA; ENSG00000162664; Tissue enhanced (retina).
DR MIM; 614601; gene.
DR neXtProt; NX_Q5BKZ1; -.
DR OpenTargets; ENSG00000162664; -.
DR PharmGKB; PA37842; -.
DR VEuPathDB; HostDB:ENSG00000162664; -.
DR eggNOG; ENOG502QUAZ; Eukaryota.
DR GeneTree; ENSGT00530000063777; -.
DR HOGENOM; CLU_024193_2_0_1; -.
DR InParanoid; Q5BKZ1; -.
DR OMA; AYPENTF; -.
DR OrthoDB; 902224at2759; -.
DR PhylomeDB; Q5BKZ1; -.
DR TreeFam; TF105407; -.
DR PathwayCommons; Q5BKZ1; -.
DR SignaLink; Q5BKZ1; -.
DR BioGRID-ORCS; 284695; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; ZNF326; human.
DR GenomeRNAi; 284695; -.
DR Pharos; Q5BKZ1; Tbio.
DR PRO; PR:Q5BKZ1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5BKZ1; protein.
DR Bgee; ENSG00000162664; Expressed in sural nerve and 185 other tissues.
DR ExpressionAtlas; Q5BKZ1; baseline and differential.
DR Genevisible; Q5BKZ1; HS.
DR GO; GO:0044609; C:DBIRD complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IMP:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR007071; AKAP95.
DR InterPro; IPR034736; ZF_C2H2_AKAP95.
DR PANTHER; PTHR12190; PTHR12190; 1.
DR Pfam; PF04988; AKAP95; 1.
DR PROSITE; PS51799; ZF_C2H2_AKAP95; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..582
FT /note="DBIRD complex subunit ZNF326"
FT /id="PRO_0000075386"
FT ZN_FING 314..336
FT /note="C2H2 AKAP95-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT ZN_FING 407..430
FT /note="C2H2 AKAP95-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT REGION 1..124
FT /note="Mediates transcriptional activation"
FT /evidence="ECO:0000250"
FT REGION 154..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 238..260
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 273..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..526
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 173
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 235
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 247
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 264
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..206
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043772"
FT VAR_SEQ 71..582
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014956"
FT CONFLICT 471
FT /note="P -> S (in Ref. 4; AAH90866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 65654 MW; 7F513DA0C5B7F3CD CRC64;
MDFEDDYTHS ACRNTYQGFN GMDRDYGPGS YGGMDRDYGH GSYGGQRSMD SYLNQSYGMD
NHSGGGGGSR FGPYESYDSR SSLGGRDLYR SGYGFNEPEQ SRFGGSYGGR FESSYRNSLD
SFGGRNQGGS SWEAPYSRSK LRPGFMEDRG RENYSSYSSF SSPHMKPAPV GSRGRGTPAY
PESTFGSRNY DAFGGPSTGR GRGRGHMGDF GSIHRPGIVV DYQNKSTNVT VAAARGIKRK
MMQPFNKPSG TFIKKPKLAK PMEKISLSKS PTKTDPKNEE EEKRRIEARR EKQRRRREKN
SEKYGDGYRM AFTCSFCKFR TFEEKDIELH LESSSHQETL DHIQKQTKFD KVVMEFLHEC
MVNKFKKTSI RKQQTNNQTE VVKIIEKDVM EGVTVDDHMM KVETVHCSAC SVYIPALHSS
VQQHLKSPDH IKGKQAYKEQ IKRESVLTAT SILNNPIVKA RYERFVKGEN PFEIQDHSQD
QQIEGDEEDE EKIDEPIEEE EDEDEEEEAE EVGEVEEVEE VEEVREGGIE GEGNIQGVGE
GGEVGVVGEV EGVGEVEEVE ELEEETAKEE PADFPVEQPE EN
